Threonine catabolism (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="Threonine catabolism" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">The degradation of L-threonine to glycine in both prokaryotes and eukaryotes takes place through a two-step biochemical pathway in mitochondria (Dale 1978). In the first step, L-threonine is oxidised to 2-amino-3-oxobutanoate. This reaction is catalysed by mitochondrial L-threonine 3-dehydrogenase tetramer (TDH tetramer). In the second step, mitochondrial 2-amino-3-ketobutyrate coenzyme A ligase (GCAT, aka KBL) catalyses the reaction between 2-amino-3-oxobutanoate and coenzyme A to form glycine and acetyl-CoA. GCAT resides on the mitochondrial inner membrane in dimeric form and requires pyridoxal 5-phosphate (PXLP) as cofactor. GCAT is thought to exist on the mitochondrial inner membrane in complex with TDH. With these two enzymes located together, it stops the rapid and spontaneous decarboxylation of 2A-3OBU to aminoacetone and carbon dioxide and instead, results in glycine formation (Tressel et al. 1986). 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In the second step, mitochondrial 2-amino-3-ketobutyrate coenzyme A ligase (GCAT, aka KBL) catalyses the reaction between 2-amino-3-oxobutanoate (2A-3OBU) and coenzyme A (CoA-SH) to form glycine (Gly) and acetyl-CoA (Ac-CoA) (Edgar &amp; Polak 2000). GCAT resides on the mitochondrial inner membrane and requires pyridoxal 5-phosphate (PXLP) as cofactor. It is strongly expressed in heart, brain, liver and pancreas. Dimeric GCAT:PXLP is thought to exist on the mitochondrial inner membrane in complex with tetrameric L-threonine 3-dehydrogenase (TDH), the first enzyme in this pathway (Tressel et al. 1986). With these two enzymes located together, it stops the rapid and spontaneous decarboxylation of 2A-3OBU to aminoacetone and carbon dioxide and instead, results in glycine formation.</Comment> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="635.0" Y="268.0" /> <Point X="738.0" Y="268.0" /> <Anchor Position="0.0" Shape="None" GraphId="e4b60" /> <Anchor Position="0.99" Shape="None" GraphId="e8a63" /> <Anchor Position="0.5" Shape="None" GraphId="c0049" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-6798345" /> </Interaction> <Interaction GraphId="c1965"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="738.0" Y="268.0" GraphRef="e8a63" RelX="1.0299999999999727" RelY="0.0" /> <Point X="755.0" Y="231.0" GraphRef="c612b" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-6798345" /> </Interaction> <Interaction GraphId="ca321"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="573.0" Y="269.0" GraphRef="c0575" RelX="1.0" RelY="0.0" /> <Point X="635.0" Y="268.0" GraphRef="e4b60" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-6798345" /> </Interaction> <Interaction GraphId="cc9a8"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="404.0" Y="474.0" GraphRef="b671f" RelX="-1.0" RelY="0.0" /> <Point X="432.0" Y="527.0" GraphRef="ab43b" RelX="2.0" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9014641" /> </Interaction> <Interaction GraphId="cfe27"> <Comment Source="Reactome">The toxic enamine/imine intermediates generated by pyridoxal 5'-phosphate (PXLP) containing enzymes can cause severe cellular damage if allowed to accumulate (Downs &amp; Ernst 2015). 2-iminobutanoate/2-iminopropanoate deaminase (RIDA aka HRSP12) is a widely conserved protein that prevents 2AA accumulation by facilitating its conversion to the stable metabolite 2-oxobutanoate (2OBUTA aka 2-ketobutyrate) (Cooper et al. 2011, Lambrecht et al. 2012, 2013, Niehaus et al. 2015).</Comment> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="353.0" Y="527.0" /> <Point X="507.0" Y="527.0" /> <Anchor Position="0.0" Shape="None" GraphId="ea8c1" /> <Anchor Position="0.99" Shape="None" GraphId="bcae5" /> <Anchor Position="0.5" Shape="None" GraphId="ab43b" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9014641" /> </Interaction> <Interaction GraphId="d4fe2"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="738.0" Y="268.0" GraphRef="e8a63" RelX="1.0299999999999727" RelY="0.0" /> <Point X="772.0" Y="298.0" GraphRef="a7b1a" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-6798345" /> </Interaction> <Interaction GraphId="dad29"> <Comment Source="Reactome">Various PXLP-dependent enzymes can catalyse α, β-elimination reactions of amino acid substrates, ultimately yielding α-keto (or 2-oxo-) acid products. However, these enzymes, such as L-serine dehydratase/L-threonine deaminase (SDS aka TDH), only form the enamine intermediate as the remainder of the reaction occurs in solution with the enamine intermediate tautomerising to the imine form, which then spontaneously hydrolyzes to the final α-keto acid product (Downs &amp; Ernst 2015). SDS can dehydrate L-threonine (L-Thr) to form the intermediate enamine 2-aminoacrylate (2AA), which can damage the pyridoxal 5'-phosphate cofactor (PXLP) of various enzymes, causing inactivation and significant cellular damage if allowed to accumulate (Lambrecht et al. 2013). SDS exists as a homodimer and requires PXLP for activity (Sun et al. 2005). 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